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• W1537820681 abstract "Research Article1 October 1996free access Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis. M. Rizzi M. Rizzi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author C. Nessi C. Nessi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author A. Mattevi A. Mattevi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author A. Coda A. Coda Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author M. Bolognesi M. Bolognesi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author A. Galizzi A. Galizzi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author M. Rizzi M. Rizzi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author C. Nessi C. Nessi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author A. Mattevi A. Mattevi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author A. Coda A. Coda Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author M. Bolognesi M. Bolognesi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author A. Galizzi A. Galizzi Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. Search for more papers by this author Author Information M. Rizzi1, C. Nessi1, A. Mattevi1, A. Coda1, M. Bolognesi1 and A. Galizzi1 1Department of Genetics and Microbiology A. Buzzati Traverso, Universityof Pavia, Italy. The EMBO Journal (1996)15:5125-5134https://doi.org/10.1002/j.1460-2075.1996.tb00896.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info NAD+ synthetase catalyzes the last step in the biosynthesis of nicotinamide adenine dinucleotide. The three-dimensional structure of NH3-dependent NAD+ synthetase from Bacillus subtilis, in its free form and in complex with ATP, has been solved by X-ray crystallography (at 2.6 and 2.0 angstroms resolution, respectively) using a combination of multiple isomorphous replacement and density modification techniques. The enzyme consists of a tight homodimer with alpha/beta subunit topology. The catalytic site is located at the parallel beta-sheet topological switch point, where one AMP molecule, one pyrophosphate and one Mg2+ ion are observed. Residue Ser46, part of the neighboring ‘P-loop’, is hydrogen bonded to the pyrophosphate group, and may play a role in promoting the adenylation of deamido-NAD+ during the first step of the catalyzed reaction. The deamido-NAD+ binding site, located at the subunit interface, is occupied by one ATP molecule, pointing towards the catalytic center. A conserved structural fingerprint of the catalytic site, comprising Ser46, is very reminiscent of a related protein region observed in glutamine-dependent GMP synthetase, supporting the hypothesis that NAD+ synthetase belongs to the newly discovered family of ‘N-type’ ATP pyrophosphatases. Previous ArticleNext Article Volume 15Issue 191 October 1996In this issue RelatedDetailsLoading ..." @default.
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• W1537820681 title "Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis." @default.
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